ID I3IZG2_ORENI Unreviewed; 1631 AA.
AC I3IZG2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Laminin, beta 2-like {ECO:0000313|Ensembl:ENSONIP00000002002.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000002002.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000002002.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR STRING; 8128.ENSONIP00000002003; -.
DR Ensembl; ENSONIT00000002001.2; ENSONIP00000002002.2; ENSONIG00000001597.2.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000167093; -.
DR OMA; EQFCIVS; -.
DR TreeFam; TF312903; -.
DR Proteomes; UP000005207; Linkage group LG20.
DR CDD; cd00055; EGF_Lam; 13.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF197; LAMININ SUBUNIT BETA-1 ISOFORM X1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 12.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT DOMAIN 34..273
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 274..337
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 338..400
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 401..460
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 461..512
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 552..763
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 769..816
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 817..862
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 863..912
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 913..971
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 972..1023
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1024..1079
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1080..1127
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1128..1174
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1444..1481
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1539..1594
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 303..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 368..377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 431..440
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 484..493
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 496..510
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 769..781
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 771..788
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 790..799
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 817..829
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 819..836
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 838..847
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 882..891
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 942..951
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 996..1005
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1052..1061
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1080..1092
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1082..1099
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1101..1110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1128..1140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1130..1147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1149..1158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1631 AA; 180539 MW; DE4E516F86DCA4B3 CRC64;
VRGMTGLADS FLMKLSSESV RTLNWLPSSP HGCTEGSCYP ATGNLLIGRA VNLTATSTCG
LNGPERYCIV SHLQVKKCFE CNSQHPYDPN VHSNSHRIEN VIYLTDSNGV NTWWQSVHGV
YESVSIRLNL EAEFHFTHLI MKFKTFRPAA LVIERSADFG RTWRPYRYYA SNCTRTFPSI
PANGLHHVND IICEERYSDI EPSTNGEVIY KVLDPAIPVK DPYRLDIQEL LRITNLRINF
TKLNTLGDDL LDRRPEVLQK YYYAIYELVV RGSCFCYGHA SECAPVPGID AREIGMIHGR
CVCKHNTEGL NCERCRNFHN DLPWRPAEAE NPHTCRECNC NGHSDQCHFD MAVYMATGNV
SGGVCDDCLH NTMGRNCETC KPFYYQDPNR DIRDPRVCVA CDCDPVGSLE GGVCDTHTDF
EMGMIAGQCR CKVNVKGTRC DDCKEGYYGL SQNDPLGCQP CNCDPRGIIV MGAPCDQISG
DCSCKRYVTG RYCNQCLPEY WGLSNDLAGC RPCDCDFGGA FNNRCMMETG QCDCRRHLIG
RQCSDVQPGY FCAPLDFYKY EAEDATGHSP PDVRTVHRER TLSHMVTWTG PGFSRVKDGA
GLVFTIDNIP YAMEYDIMIR YEPEVCEYGE NMMGGFLVES KSKIKYKIHL LLHVLSCSMC
SYRYIQMPRP FCFEPSNRYV VTVRFQRHGA THRHLTAFIL IDSLVLIPKY TELPGFQGNT
PESEQRQEEM IRYMCLDSFM ITPMPALAEM CSKLICSISS IIHDGALPCE CDPQGSLSGE
CDVVGGQCRC KPNVIGRRCD QCAPGTYGFG VSGCTACDCH SDGSLSHQCD PVTGQCQCRQ
GATGRQCSDC QPGQWGFPSC TPCQCNGHAD LCDPRTGECR GCRDFTAGHL CERCMDTFFG
NPALGSGQHC RPCPCPNNPN SDNFNALSCQ VDHTSDQIMC NCKQGYMGLR CDQCAPGYYG
NPEQPGGQCF PCECNGNIDT QDPESCDPRT GECIKCLYHT DGPSCAQCQN GYYGNALAHD
CRRCTCVTAG TLQSACSDGH CDCDRQTGAC PCREHVVGHN CDQCAPNYWN FGQDRGCEPC
NCNSQHALGS HCNMFTGQCH CHSGFGGKQC TECELFHWGD PREQCHECNC NPEGAEISQC
DRLTGACECR EGATGLQCNQ CARGFTGIFP KCIQCHPCFQ LWDDAVCQIR RDLDHIQSRV
QEILKGGIIP GAGDARIKEL EGKLKQVKDL IITQDRDRVY QLIGQSIDDL RWGNSSLSFV
VSHHLTAVNT GSRLNPYPLL VFLTDQFEKV KQYYQESLEA EMKCNASVFG PMSPLEESNK
IRARTENLLD ETENDINRNV ASCCPALNLI PLTQSVHGAI FKVCGGHSNS SVNGSCPDSR
CGGAGCHDDQ GNRVCGGVGC SGTVGTSVAA LNDARNVTDS LNTASKELQK VSKKDIAAMT
QNLKNQTINT LEKANKLSKE LKESNKNLTE FIEKIKNFLT EEGADPESIE KVAQEVLSIT
LPLNRTVLDK MIAQIKESLS NIGNIEGIVN QTTLHTTKVK ELLDAAKQAK RRAEEVKDMT
NITKEALKAS GKAIEKAQAA LKEAHNNLNS TRNATAEVQN PGTCKFTGFT YFLSSTSPMS
TFVHFTSVLF I
//
